Analytical Data
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Gene name
UBA3/APPBP1
- Application
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Species
Triticum aestivum
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Source
E. coli
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Tag
N- His-KSI
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31252
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Expression Region
429-639aa
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Molecular Weight
38.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
UBA3/APPBP1 is a critical protein complex involved in various cellular processes, particularly in the ubiquitin-proteasome system, which regulates protein degradation and quality control. UBA3, a ubiquitin-activating enzyme, forms a heterodimer with APPBP1, facilitating the conjugation of ubiquitin to target proteins, thereby signaling for their degradation. Research has shown that this complex plays a vital role in maintaining cellular homeostasis and responding to stress. Dysregulation of UBA3/APPBP1 has been implicated in several diseases, including cancer and neurodegenerative disorders, as it can affect apoptosis, cell cycle regulation, and protein aggregation. Understanding the biochemical mechanisms and interactions of UBA3/APPBP1 not only sheds light on fundamental cellular processes but also provides potential therapeutic targets for correcting the malfunction of these pathways in various diseases. Current studies focus on elucidating the structural characteristics of the UBA3/APPBP1 complex, identifying its substrates, and exploring its role in protein homeostasis. This research is critical for advancing our knowledge of cellular regulation and the development of novel strategies for disease intervention.
